Abstract:
:The yolk platelets from Rhodnius prolixus, a blood-sucking bug, are composed mostly of vitellin and here are shown to contain at least two hydrolytic enzymes, a phosphatase and a cathepsin D-like proteinase. Both the proteinase and the phosphatase have an acid pH optimum. No hydrolytic activity was observed under alkaline or neutral conditions. Among several proteinase inhibitors tested, only pepstatin could abolish vitellin breakdown in vitro. The proteinase appears to be bound to the yolk platelet membranes. The phosphatase activity, using p-nitrophenyl phosphate as substrate, was enhanced after disruption of the platelet membrane by Triton X-100. This activity could be inhibited by tartrate but not by p-cloromercuribenzoate.
journal_name
Arch Insect Biochem Physioljournal_title
Archives of insect biochemistry and physiologyauthors
Nussenzveig RH,Oliveira PL,Masuda Hdoi
10.1002/arch.940210402subject
Has Abstractpub_date
1992-01-01 00:00:00pages
253-62issue
4eissn
0739-4462issn
1520-6327journal_volume
21pub_type
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